References
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58. Lee SJ, McCormick MS, Lippard SJ, Cho US (2013) Control of substrate access to the active
site in methane monooxygenase. Nature 494:380–384
59. Wang W, Lippard SJ (2014) Diiron oxidation state control of substrate access to the active
site of soluble methane monooxygenase mediated by the regulatory component. J Am Chem
Soc 136:2244–2247
60. Lund J, Woodland MP, Dalton H (1985) Electron transfer reactions in the soluble methane
monooxygenase of Methylococcus capsulatus (Bath). Eur J Biochem 147:297–305
61. Blazyk JL, Lippard SJ (2002) Expression and characterization of ferredoxin and flavin adenine
dinucleotide binding domains of the reductase component of soluble methane monooxygenase
from Methylococcus capsulatus (Bath). Biochemistry 41:15780–15794
62. Müller J, Lugovskoy AA, Wagner G, Lippard SJ (2002) NMR structure of the [2Fe-2S]
ferredoxin domain from soluble methane monooxygenase reductase and interaction with its
hydroxylase. Biochemistry 41:42–51
63. Gassner GT, Lippard SJ (1999) Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38:12768–12785
64. Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD (1997) Roles of the methane
monooxygenase reductase component in the regulation of catalysis. Biochemistry 36:5223–
5233
65. Kopp DA, Berg EA, Costello CE, Lippard SJ (2003) Structural features of covalently crosslinked hydroxylase and reductase proteins of soluble methane monooxygenase as revealed by
mass spectrometric analysis. J Biol Chem 278:20939–20945
66. Fox BG, Liu Y, Dege JE, Lipscomb JD (1991) Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification
of sites of component interaction. J Biol Chem 266:540–550
67. Wang W, Iacob RE, Luoh RP, Engen JR, Lippard SJ (2014) Electron transfer control in soluble
methane monooxygenase. J Am Chem Soc 136:9754–9762
68. Paulsen KE, Liu Y, Fox BG, Lipscomb JD, Münck E, Stankovich MT (1994) Oxidationreduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry 33:713–722
69. Liu KE, Lippard SJ (1991) Redox properties of the hydroxylase component of methane
monooxygenase from Methylococcus capsulatus (Bath). Effects of protein B, reductase, and
substrate. J Biol Chem 266:12836–12839
70. lazyk JL, Gassner GT, Lippard SJ (2005) Intermolecular electron-transfer reactions in soluble methane monooxygenase: a role for hysteresis in protein function. J Am Chem Soc
127:17364–17376
71. Froland WA, Andersson KK, Lee SK, Liu Y, Lipscomb JD (1992) Methane monooxygenase
component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed
reactions. J Biol Chem 267:17588–17597
72. Liu Y, Nesheim JC, Lee SK, Lipscomb JD (1995) Gating effects of component B on oxygen
activation by the methane monooxygenase hydroxylase component. J Biol Chem 270:24662–
24665
73. MacArthur R, Sazinsky MH, Kühne H, Whittington DA, Lippard SJ, Brudvig GW (2002)
Component B binding to the soluble methane monooxygenase hydroxylase by saturationrecovery EPR spectroscopy of spin-labeled MMOB. J Am Chem Soc 124:13392–13393
74. Brazeau BJ, Wallar BJ, Lipscomb JD (2003) Effector proteins from P450 (cam) and methane
monooxygenase: lessons in tuning nature’s powerful reagents. Biochem Biophys Res
Commun 312:143–148
75. Zhang JY, Wallar BJ, Popescu CV, Renner DB, Thomas DD, Lipscomb JD (2006) Methane
monooxygenase hydroxylase and B component interactions. Biochemistry 45:2913–2926
76. Lee SJ (2016) Hydroxylation of methane through component interactions in soluble methane
monooxygenases. J Microbiol 54:277–282
77. Wang W, Liang AD, Lippard SJ (2015) Coupling oxygen consumption with hydrocarbon
oxidation in bacterial multicomponent monooxygenases. Acc Chem Res 48:2632–2639
49
58. Lee SJ, McCormick MS, Lippard SJ, Cho US (2013) Control of substrate access to the active
site in methane monooxygenase. Nature 494:380–384
59. Wang W, Lippard SJ (2014) Diiron oxidation state control of substrate access to the active
site of soluble methane monooxygenase mediated by the regulatory component. J Am Chem
Soc 136:2244–2247
60. Lund J, Woodland MP, Dalton H (1985) Electron transfer reactions in the soluble methane
monooxygenase of Methylococcus capsulatus (Bath). Eur J Biochem 147:297–305
61. Blazyk JL, Lippard SJ (2002) Expression and characterization of ferredoxin and flavin adenine
dinucleotide binding domains of the reductase component of soluble methane monooxygenase
from Methylococcus capsulatus (Bath). Biochemistry 41:15780–15794
62. Müller J, Lugovskoy AA, Wagner G, Lippard SJ (2002) NMR structure of the [2Fe-2S]
ferredoxin domain from soluble methane monooxygenase reductase and interaction with its
hydroxylase. Biochemistry 41:42–51
63. Gassner GT, Lippard SJ (1999) Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38:12768–12785
64. Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD (1997) Roles of the methane
monooxygenase reductase component in the regulation of catalysis. Biochemistry 36:5223–
5233
65. Kopp DA, Berg EA, Costello CE, Lippard SJ (2003) Structural features of covalently crosslinked hydroxylase and reductase proteins of soluble methane monooxygenase as revealed by
mass spectrometric analysis. J Biol Chem 278:20939–20945
66. Fox BG, Liu Y, Dege JE, Lipscomb JD (1991) Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification
of sites of component interaction. J Biol Chem 266:540–550
67. Wang W, Iacob RE, Luoh RP, Engen JR, Lippard SJ (2014) Electron transfer control in soluble
methane monooxygenase. J Am Chem Soc 136:9754–9762
68. Paulsen KE, Liu Y, Fox BG, Lipscomb JD, Münck E, Stankovich MT (1994) Oxidationreduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry 33:713–722
69. Liu KE, Lippard SJ (1991) Redox properties of the hydroxylase component of methane
monooxygenase from Methylococcus capsulatus (Bath). Effects of protein B, reductase, and
substrate. J Biol Chem 266:12836–12839
70. lazyk JL, Gassner GT, Lippard SJ (2005) Intermolecular electron-transfer reactions in soluble methane monooxygenase: a role for hysteresis in protein function. J Am Chem Soc
127:17364–17376
71. Froland WA, Andersson KK, Lee SK, Liu Y, Lipscomb JD (1992) Methane monooxygenase
component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed
reactions. J Biol Chem 267:17588–17597
72. Liu Y, Nesheim JC, Lee SK, Lipscomb JD (1995) Gating effects of component B on oxygen
activation by the methane monooxygenase hydroxylase component. J Biol Chem 270:24662–
24665
73. MacArthur R, Sazinsky MH, Kühne H, Whittington DA, Lippard SJ, Brudvig GW (2002)
Component B binding to the soluble methane monooxygenase hydroxylase by saturationrecovery EPR spectroscopy of spin-labeled MMOB. J Am Chem Soc 124:13392–13393
74. Brazeau BJ, Wallar BJ, Lipscomb JD (2003) Effector proteins from P450 (cam) and methane
monooxygenase: lessons in tuning nature’s powerful reagents. Biochem Biophys Res
Commun 312:143–148
75. Zhang JY, Wallar BJ, Popescu CV, Renner DB, Thomas DD, Lipscomb JD (2006) Methane
monooxygenase hydroxylase and B component interactions. Biochemistry 45:2913–2926
76. Lee SJ (2016) Hydroxylation of methane through component interactions in soluble methane
monooxygenases. J Microbiol 54:277–282
77. Wang W, Liang AD, Lippard SJ (2015) Coupling oxygen consumption with hydrocarbon
oxidation in bacterial multicomponent monooxygenases. Acc Chem Res 48:2632–2639